RNA aptamers specifically interact with the prion protein PrP.
about
Unique quadruplex structure and interaction of an RNA aptamer against bovine prion proteinA G-quadruplex–containing RNA activates fluorescence in a GFP-like fluorophoreA visual dual-aptamer logic gate for sensitive discrimination of prion diseases-associated isoform with reusable magnetic microparticles and fluorescence quantum dotsRNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivityInduced prion protein controls immune-activated retroviruses in the mouse spleenCancer-selective antiproliferative activity is a general property of some G-rich oligodeoxynucleotides.The intriguing prion disorders.Heparin binding confers prion stability and impairs its aggregation.Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.Rapid detection of natriuretic peptides by a microfluidic LabChip analyzer with DNA aptamers: Application of natriuretic peptide detection.Different conformations of phosphatase and tensin homolog, deleted on chromosome 10 (PTEN) protein within the nucleus and cytoplasm of neuronsLipopolysaccharide induced conversion of recombinant prion protein.Engineering the quadruplex fold: nucleoside conformation determines both folding topology and molecularity in guanine quadruplexes.DNA aptamers against exon v10 of CD44 inhibit breast cancer cell migration.Local neutral networks help maintain inaccurately replicating ribozymesPrion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth.Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation.Anti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its beta isoform with high affinityImmunoassays with rolling circle DNA amplification: a versatile platform for ultrasensitive antigen detection.Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of beta-secretase BACE1 in vitro.Aptamers recognizing glycosylated hemagglutinin expressed on the surface of vaccinia virus-infected cells.Selection of aptamers for amyloid beta-protein, the causative agent of Alzheimer's disease.Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells.Implications of peptide assemblies in amyloid diseases.Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cellsRNA aptamers selected against the receptor activator of NF-kappaB acquire general affinity to proteins of the tumor necrosis factor receptor family.Disease-associated prion protein elicits immunoglobulin M responses in vivoBinding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells.Smart protein biogate as a mediator to regulate competitive host-guest interaction for sensitive ratiometric electrochemical assay of prion.Case for an RNA-prion world: a hypothesis based on conformational diversity.Screening of DNA aptamer against mouse prion protein by competitive selection.Aptamers Selected for Recognizing Amyloid β-Protein-A Case for Cautious Optimism.
P2860
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P2860
RNA aptamers specifically interact with the prion protein PrP.
description
1997 nî lūn-bûn
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1997年の論文
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年學術文章
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1997年學術文章
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name
RNA aptamers specifically interact with the prion protein PrP.
@en
type
label
RNA aptamers specifically interact with the prion protein PrP.
@en
prefLabel
RNA aptamers specifically interact with the prion protein PrP.
@en
P2093
P2860
P1433
P1476
RNA aptamers specifically interact with the prion protein PrP
@en
P2093
Groschup MH
Kretzschmar HA
Winnacker EL
P2860
P304
P407
P577
1997-11-01T00:00:00Z